4tm7

Publication Abstract from PubMed

As an alternative to Darwinian evolution relying on catalytic promiscuity, a protein may acquire auxiliary function upon metal binding, thus providing it with a novel catalytic machinery. Here we show that addition of cupric ions to a 6-phosphogluconolactonase 6-PGLac bearing a putative metal binding site leads to the emergence of peroxidase activity (kcat 7.8 x 10(-2) s(-1), KM 1.1 x 10(-5) M). Both X-ray crystallographic and EPR data of the copper-loaded enzyme Cu.6-PGLac reveal a bis-histidine coordination site, located within a shallow binding pocket capable of accommodating the o-dianisidine substrate.

Enzyme repurposing of a hydrolase as an emergent peroxidase upon metal binding.,Fujieda N, Schatti J, Stuttfeld E, Ohkubo K, Maier T, Fukuzumi S, Ward TR Chem Sci. 2015 Jul 1;6(7):4060-4065. doi: 10.1039/c5sc01065a. Epub 2015 May 7. PMID:29218172^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.